Reviewed, UniProtKB/Swiss-Prot A8A7U4 (ULAF_ECOHS)

Names and origin

Protein names

Recommended name:
    L-ribulose-5-phosphate 4-epimerase ulaF
    EC=5.1.3.4
Alternative name(s):
    Phosphoribulose isomerase
    L-ascorbate utilization protein F

Gene names

Name:	ulaF
Ordered Locus Names:	EcHS_A4442

Organism

Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]

Taxonomic identifier

331112 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the isomerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization By similarity.
Catalytic activity	L-ribulose 5-phosphate = D-xylulose 5-phosphate. HAMAP MF_01952
Cofactor	Binds 1 zinc ion per subunit Potential.
Pathway	Cofactor degradation; L-ascorbate degradation; D-xylulose 5-phosphate from L-ascorbate: step 4/4. HAMAP MF_01952
Induction	Induced by L-ascorbate. Repressed by ulaR By similarity.
Sequence similarities	Belongs to the aldolase class II family. AraD/fucA subfamily.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-ascorbic acid metabolic process Inferred from electronic annotation. Source: HAMAP
Molecular function	L-ribulose-phosphate 4-epimerase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 228	228	L-ribulose-5-phosphate 4-epimerase ulaF HAMAP MF_01952		PRO_1000070637
Sites
	Metal binding	74	1	Zinc By similarity
	Metal binding	93	1	Zinc By similarity
	Metal binding	95	1	Zinc By similarity
	Metal binding	167	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8A7U4-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: A9F842F35008EE98	FASTA	228	25,338
	10 20 30 40 50 60 MQKLKQQVFE ANMDLPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KADDMVVVDM 70 80 90 100 110 120 SGKVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT AWAQAGLAIP ALGTTHADYF 130 140 150 160 170 180 FGDIPCTRGL SEEEVQGEYE LNTGKVIIET LGNAEPLHTP GIVVYQHGPF AWGKDAHDAV 190 200 210 220 HNAVVMEEVA KMAWIARSIN PQLNHIDSFL MNKHFMRKHG PNAYYGQK

References

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000802 Genomic DNA. Translation: ABV08598.1.
RefSeq	YP_001460981.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A8A7U4.
Genome annotation databases
GeneID	5595326.
GenomeReviews	Gene locus EcHS_A4442 in contig CP000802_GR.
KEGG	ecx:EcHS_A4442.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	DAEPLHT.
Family and domain databases
HAMAP	MF_01952. [Tree]
InterPro	IPR001303. Aldolase_II/adducin_N. [Graphical view]
Gene3D	G3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit.
Pfam	PF00596. Aldolase_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ULAF_ECOHS

Accession

Primary (citable) accession number: A8A7U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	November 3, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)